3-mercaptopyruvate sulfurtransferase: Difference between revisions

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| Name = biotin synthase
| EC_number = 2.8.1.6
| CAS_number = 80146-93-6
| IUBMB_EC_number = 2/8/1/6
| GO_code = 0004076
| image =
| width =
| caption =
}}
In [[enzymology]], a '''biotin synthase''' ({{EC number|2.8.1.6}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:dethiobiotin + sulfur + 2 S-adenosyl-L-methionine <math>\rightleftharpoons</math> biotin + 2 L-methionine + 2 5'-deoxyadenosine
 
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[dethiobiotin]], [[sulfur]], and [[S-adenosyl-L-methionine]], whereas its 3 [[product (chemistry)|products]] are [[biotin]], [[L-methionine]], and [[5'-deoxyadenosine]].
 
This [[radical SAM]] enzyme belongs to the family of [[transferase]]s, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is '''dethiobiotin:sulfur sulfurtransferase'''. This enzyme participates in [[biotin metabolism]].  It employs one [[cofactor (biochemistry)|cofactor]], [[iron-sulfur]].
 
==Structural studies==
 
As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|1R30}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = Shiuan D, Campbell A | date = 1988 | title = Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons | journal = Gene. | volume = 67 | pages = 203&ndash;11  | pmid = 2971595 | doi = 10.1016/0378-1119(88)90397-6 | issue = 2 }}
* {{cite journal | author = Zhang S, Sanyal I, Bulboaca GH, Rich A, Flint DH | date = 1994 | title = The gene for biotin synthase from Saccharomyces cerevisiae: cloning, sequencing, and complementation of Escherichia coli strains lacking biotin synthase | journal = Arch. Biochem. Biophys. | volume = 309 | pages = 29&ndash;35  | pmid = 8117110 | doi = 10.1006/abbi.1994.1079 | issue = 1 }}
* {{cite journal | author = Trainor DA, Parry RJ and Gitterman A | date = 1980 | title = Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at C-4 of dethiobiotin | journal = J. Am. Chem. Soc.  | volume = 102 | pages = 1467&ndash;1468 | doi = 10.1021/ja00524a064 | issue = 4 }}
* {{cite journal | author = Lotierzo M, Tse Sum Bui B, Florentin D, Escalettes F, Marquet A | date = 2005 | title = Biotin synthase mechanism: an overview | journal = Biochem. Soc. Trans. | volume = 33 | pages = 820&ndash;3  | pmid = 16042606 | doi = 10.1042/BST0330820 | issue = Pt 4 }}
* {{cite journal | author = Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL | date = 2004 | title = Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme | journal = Science. | volume = 303 | pages = 76&ndash;9  | pmid = 14704425 | doi = 10.1126/science.1088493 | issue = 5654 | pmc = 1456065 }}
* {{cite journal | author = Ugulava NB, Gibney BR, Jarrett JT | date = 2001 | title = Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions | journal = Biochemistry. | volume = 40 | pages = 8343&ndash;51  | pmid = 11444981 | doi = 10.1021/bi0104625 | issue = 28 | pmc = 1538964 }}
 
{{transferase-stub}}
 
[[Category:EC 2.8.1]]
[[Category:Iron-sulfur enzymes]]
[[Category:Enzymes of known structure]]

Latest revision as of 21:41, 28 July 2014

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